Concept explainers
(a)
Interpretation: The meaning of the notation “ES” in the given equation has to be stated.
Concept introduction: The binding of the substrate to the active site of the enzyme results in the formation of enzyme-substrate complex. The catalysis of enzyme-substrate complex produces enzyme-product complex. It dissociates to give free enzyme and product.
(b)
Interpretation: The meaning of the notation “P” in the given equation has to be stated.
Concept introduction: The binding of the substrate to the active site of the enzyme results in the formation of enzyme-substrate complex. The catalysis of enzyme-substrate complex produces enzyme-product complex. It dissociates to give free enzyme and product.
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Chapter 21 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- what is the purpose of staggering the start and stop of the reactions? With reference to your experimental protocol, what is the purpose of staggering the start and stop of the reactions? A.To ensure that the reaction occurs with different amounts of enzyme in each tube so as to ensure comparability between reaction tubes. B.To ensure that the reaction occurs at exactly the same pH in each tube so as to ensure comparability between reaction tubes. C.To ensure that the reaction occurs for exactly the same time interval (30 minutes) in each tube so as to ensure comparability between reaction tubes. D.To ensure that the reaction occurs with exactly the same amount of substrate in each tube so as to ensure comparability between reaction tubes.arrow_forwardMost of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: Give the Michaelis-Menten equation of an enzyme reaction and draw the Michaelis-Menten plot of [S] versus V0.arrow_forwardDuring the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.arrow_forward
- The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"arrow_forwardAn enzyme contains an active site aspartic acid with a pK, = 5.0, which acts as a general acid catalyst. On the template below, draw the curve of enzyme activity (reaction rate) vs. pH for the enzyme (assume the protein is stably folded between pH 2–12 and that the active site Asp is the only ionizable residue involved in catalysis). Briefly explain the shape of your curve.arrow_forwardExplain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal for determining KM for an enzymecatalyzed reaction that follows Michaelis–Menten kinetics.arrow_forward
- The following questions deal with a fundamental understanding of enzyme catalysis.a. Why is the rate of an enzyme-catalyzed reaction proportional to the amount of (ES) complex?b. What do you think is meant by saturation of the enzyme?c. What do you think is meant by the term “saturation kinetics”?d. How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reachesa maximum value at high [S]?arrow_forwardYou have obtained experimental kinetic data for two versions of the same enzyme, a wild‑type and a mutant differing from the wild‑type at a single amino acid. The data are given in the table. Compare the kinetic parameters of the two versions using the data in the table. Assuming a two-step reaction scheme in which ?−1 is much larger than ?2, which of the following statements are correct? The mutant version has a higher affinity for the substrate. The wild‑type version requires a greater concentration of substrate to achieve ?maxVmax. The wild‑type version has a higher affinity for the substrate. The mutant version requires a greater concentration of substrate to achieve ?maxVmax. Calculate the initial velocity of the reaction catalyzed by the wild‑type enzyme when the substrate concentration is 10 mM. The reaction equilibrium is reached once there is no net change in the concentration of the substrate or the product. Based on the data table and your initial…arrow_forwardThe Lineweaver-Burke plot was originally developed in order to "linearize" the data obtained from enzyme kinetics experiments, in order to facilitate the determination of kinetic parameters. Why is it not considered to be an accurate method for this purpose? It is very difficult to draw a straight line on a computer. It is very difficult to calculate the variables required for the "x" and "y" axis. It is more accurate to use the standard "V versus [S]" plot to determine Vmax and KM- The plot weights the least accurate data points the most heavily. It is no longer considered to be acceptable to extrapolate from known data.arrow_forward
- Given the following data in enzyme-catalyzed reaction, what are the Vm, Km of with DEDS (presence of inhibitor) and without DEDS ( absence of inhibitor) and its type of inhibition.arrow_forwardIn enzyme kinetics, for the reversible with one complex mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicates forward direction while the variables denoted with b indicate backward direction.arrow_forwardIn enzyme kinetics, for the reversible with two central complexes mechanism, please provide complete proof that the rate equation is the equation below. The variables denoted with f indicate forward direction while the variables denoted with b indicate backward direction.arrow_forward
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